A flagellum is a hairlike appendage that protrudes from a wide range of microorganisms termed as flagellates. A flagellate can have one or several flagella. Certain other cells are flagellated, such as the mammalian sperm cell, which uses its flagellum to propel itself through the female reproductive tract. The primary function of a flagellum is that of motility. In some bacteria the flagellum can also function as a sensory organelle, being sensitive to wetness, chemicals, and temperatures outside the cell.
A sigma factor is a protein needed for initiation of transcription in bacteria. It is a bacterial transcription initiation factor that enables specific binding of RNA polymerase (RNAP) to gene promoters. It is homologous to archaeal transcription factor B and to eukaryotic factor TFIIB. The specific sigma factor used to initiate transcription of a given gene will vary, depending on the gene and on the environmental signals needed to initiate transcription of that gene. Selection of promoters by RNA polymerase is dependent on the sigma factor that associates with it. They are also found in plant chloroplasts as a part of the bacteria-like plastid-encoded polymerase (PEP).
The L-ring of the bacterial flagellum is the ring in the lipid outer cell membrane through which the axial filament passes. that l ring stands for lipopolysaccharide.
In enzymology, a protein-glutamate O-methyltransferase is an enzyme that catalyzes the chemical reaction
Cobalt chelatase (EC 6.6.1.2) is an enzyme that catalyzes the chemical reaction
In enzymology, a nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase is an enzyme that catalyzes the chemical reaction
The CorA transport system is the primary Mg2+ influx system of Salmonella typhimurium and Escherichia coli. CorA is ubiquitous in the Bacteria and Archaea. There are also eukaryotic members of the family localized to the mitochondrial membrane such as MRS2 and Lpe10 in yeast.
Motility protein A, MotA, is a bacterial protein that is encoded by the motA gene. It is a component of the flagellar motor. More specifically, MotA and MotB make the stator of a H+ driven bacterial flagella and surround the rotor as a ring of about 8–10 particles. MotA and MotB are integral membrane proteins. MotA has four transmembrane domains.
Motility protein B also known as MotB is a bacterial protein that is encoded by the motB gene. It's a component of the flagellar motor. More specifically, MotA and MotB makes the stator of a flagellum and surround the rotor as a ring of about 8-10 particles. MotA and MotB are integral membrane proteins. While both MotA and MotB surround the MS ring, MotB also anchors MotA to cell wall peptidoglycan. These two proteins form pores that harvest energy for flagellar mechanical movement by proton motive force (PMF) across the membrane. Cellular metabolic processes such as the electron transport chain move protons outside the cell, creating more protons and more positive charge in the extracellular space. When the protons flow back into the cell through MotA and MotB along concentration and charge gradients, they release energy that is used for flagellar rotation. The speed of the flagellar motor is dependent on the magnitude of the PMF acting on MotA and MotB.
The Methyl-accepting chemotaxis proteins are a family of transmembrane receptors that mediate chemotactic response in certain enteric bacteria, such as Salmonella typhimurium and Escherichia coli. These methyl-accepting chemotaxis receptors are one of the first components in the sensory excitation and adaptation responses in bacteria, which act to alter swimming behaviour upon detection of specific chemicals. Use of the MCP allows bacteria to detect concentrations of molecules in the extracellular matrix so that the bacteria may smooth swim or tumble accordingly. If the bacterium detects rising levels of attractants (nutrients) or declining levels of repellents (toxins), the bacterium will continue swimming forward, or smooth swimming. If the bacterium detects declining levels of attractants or rising levels of repellents, the bacterium will tumble and re-orient itself in a new direction. In this manner, a bacterium may swim towards nutrients and away from toxins
The PilZ protein family is named after the type IV pilus control protein first identified in Pseudomonas aeruginosa, expressed as part of the pil operon. It has a cytoplasmic location and is essential for type IV fimbrial, or pilus, biogenesis. PilZ is a c-di-GMP binding domain and PilZ domain-containing proteins represent the best studied class of c-di-GMP effectors. C-di-GMP, cyclic diguanosine monophosphate, the second messenger in cells, is widespread in and unique to the bacterial kingdom. Elevated intracellular levels of c-di-GMP generally cause bacteria to change from a motile single-cell state to a sessile, adhesive surface-attached multicellular state called biofilm.
In molecular biology, the ter site, also known as DNA replication terminus binding-site, refers to a protein domain which binds to the DNA replication terminus site. Ter-binding proteins are found in some bacterial species, and include the tus protein which is part of the common ter-tus binding domain. They are required for the termination of DNA replication and function by binding to DNA replication terminator sequences, thus preventing the passage of replication forks. The termination efficiency is affected by the affinity of a particular protein for the terminator sequence.
In molecular biology, the arginine repressor (ArgR) is a repressor of prokaryotic arginine deiminase pathways.
In molecular biology, the ars operon is an operon found in several bacterial taxon. It is required for the detoxification of arsenate, arsenite, and antimonite. This system transports arsenite and antimonite out of the cell. The pump is composed of two polypeptides, the products of the arsA and arsB genes. This two-subunit enzyme produces resistance to arsenite and antimonite. Arsenate, however, must first be reduced to arsenite before it is extruded. A third gene, arsC, expands the substrate specificity to allow for arsenate pumping and resistance. ArsC is an approximately 150-residue arsenate reductase that uses reduced glutathione (GSH) to convert arsenate to arsenite with a redox active cysteine residue in the active site. ArsC forms an active quaternary complex with GSH, arsenate, and glutaredoxin 1 (Grx1). The three ligands must be present simultaneously for reduction to occur.
In molecular biology, cob(I)yrinic acid a,c-diamide adenosyltransferase EC 2.5.1.17 is an enzyme which catalyses the conversion of cobalamin into one of its coenzyme forms, adenosylcobalamin. Adenosylcobalamin is required as a cofactor for the activity of certain enzymes. AdoCbl contains an adenosyl moiety liganded to the cobalt ion of cobalamin via a covalent Co-C bond.
In molecular biology, glycoside hydrolase family 73 is a family of glycoside hydrolases.
Histone-like nucleoid-structuring protein (H-NS), is one of twelve nucleoid-associated proteins (NAPs) whose main function is the organization of genetic material, including the regulation of gene expression via xenogeneic silencing. H-NS is characterized by an N-terminal domain (NTD) consisting of two dimerization sites, a linker region that is unstructured and a C-terminal domain (CTD) that is responsible for DNA-binding. Though it is a small protein, this protein provides essential nucleoid compaction and regulation of genes and is highly expressed, functioning as a dimer or multimer. Change in temperature causes H-NS to be dissociated from the DNA duplex, allowing for transcription by RNA polymerase, and in specific regions lead to pathogenic cascades in enterobacteria such as Escherichia coli and the four Shigella species.
In molecular biology, the OmpA domain is a conserved protein domain with a beta/alpha/beta/alpha-beta(2) structure found in the C-terminal region of many Gram-negative bacterial outer membrane proteins, such as porin-like integral membrane proteins, small lipid-anchored proteins, and MotB proton channels. The N-terminal half of these proteins is variable although some of the proteins in this group have the OmpA-like transmembrane domain at the N terminus. OmpA from Escherichia coli is required for pathogenesis, and can interact with host receptor molecules. MotB serve two functions in E. coli, the MotA(4)-MotB(2) complex attaches to the cell wall via MotB to form the stator of the flagellar motor, and the MotA-MotB complex couples the flow of ions across the cell membrane to movement of the rotor.
CsgD is a transcription and response regulator protein referenced to as the master modulator of bacterial biofilm development. In E. coli cells, CsgD is tasked with aiding the transition from planktonic cell motility to the stationary phase of biofilm formation, in response to environmental growth factors. A transcription analysis assay illustrated a heightened decrease in CsgD's DNA-binding capacity when phosphorylated at A.A. D59 of the protein's primary sequence. Therefore, in the protein's active form (unphosphorylated), CsgD is capable of carrying out its normal functions of regulating curli proteins (fimbria) and producing ECM polysaccharides (cellulose). Following a promoter-lacZ fusion assay of CsgD binding to specific target sites on E. coli's genome, two classes of binding targets were identified: group I genes and group II genes. The group I genes, akin to fliE and yhbT, exhibit repressed transcription following their interaction with CsgD, whilst group II genes, including yccT and adrA, illustrated active functionality. Other group I operons that illustrate repressed transcription include fliE and fliEFGH, for motile flagellum formation. Other group II genes, imperative to the transition towards stationary biofilm development, include csgBA, encoding for curli fimbriae, and adrA, encoding for the synthesis of cyclic diguanylate. In this context, c-di-GMP functions as a bacterial secondary messenger, enhancing the production of extracellular cellulose and impeding flagellum production and rotation.
Michael Eisenbach, Ph.D., is an Israeli biochemist who specializes in the navigation mechanisms of bacterial and sperm cells. He is a professor emeritus at the Weizmann Institute of Science, Department of Biomolecular Sciences, Rehovot, Israel. He discovered that sperm cells (spermatozoa) of mammals are actively guided to the egg. This opened the research field of mammalian sperm navigation. He demonstrated that the active navigation entails chemotaxis and thermotaxis. He made seminal contributions to the understanding of these two processes at the molecular, physiological and behavioural levels, as well as contributing to our understanding of the molecular mechanism of bacterial chemotaxis.
